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Tumor necrosis factor ligand superfamily member 13B (B lymphocyte stimulator) (BLyS) (B-cell-activating factor) (BAFF) (Dendritic cell-derived TNF-like molecule) (TNF- and APOL-related leukocyte expressed ligand 1) (TALL-1) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form]

 TN13B_HUMAN             Reviewed;         285 AA.
Q9Y275; E0ADT7; Q6FHD6; Q7Z5J2;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 182.
RecName: Full=Tumor necrosis factor ligand superfamily member 13B;
AltName: Full=B lymphocyte stimulator;
Short=BLyS;
AltName: Full=B-cell-activating factor;
AltName: Full=BAFF;
AltName: Full=Dendritic cell-derived TNF-like molecule;
AltName: Full=TNF- and APOL-related leukocyte expressed ligand 1;
Short=TALL-1;
AltName: CD_antigen=CD257;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 13b, membrane form;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 13b, soluble form;
Name=TNFSF13B; Synonyms=BAFF, BLYS, TALL1, TNFSF20, ZTNF4;
ORFNames=UNQ401/PRO738;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10331498;
Shu H.-B., Hu W.-H., Johnson H.;
"TALL-1 is a novel member of the TNF family that is down-regulated by
mitogens.";
J. Leukoc. Biol. 65:680-683(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
134-148.
PubMed=10359578; DOI=10.1084/jem.189.11.1747;
Schneider P., MacKay F., Steiner V., Hofmann K., Bodmer J.-L.,
Holler N., Ambrose C., Lawton P., Bixler S., Acha-Orbea H.,
Valmori D., Romero P., Werner-Favre C., Zubler R.H., Browning J.L.,
Tschopp J.;
"BAFF, a novel ligand of the tumor necrosis factor family, stimulates
B cell growth.";
J. Exp. Med. 189:1747-1756(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Monocyte, and Neutrophil;
PubMed=10398604; DOI=10.1126/science.285.5425.260;
Moore P.A., Belvedere O., Orr A., Pieri K., LaFleur D.W., Feng P.,
Soppet D., Charters M., Gentz R., Parmelee D., Li Y., Galperina O.,
Giri J., Roschke V., Nardelli B., Carrell J., Sosnovtseva S.,
Greenfield W., Ruben S.M., Olsen H.S., Fikes J., Hilbert D.M.;
"BLyS: member of the tumor necrosis factor family and B lymphocyte
stimulator.";
Science 285:260-263(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
SUBUNIT.
PubMed=12867412; DOI=10.1074/jbc.M306852200;
Gavin A.L., Ait-Azzouzene D., Ware C.F., Nemazee D.;
"DeltaBAFF, an alternate splice isoform that regulates receptor
binding and biopresentation of the B cell survival cytokine, BAFF.";
J. Biol. Chem. 278:38220-38228(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), SUBUNIT,
AND ALTERNATIVE SPLICING.
PubMed=22749832; DOI=10.1016/j.jaut.2012.05.009;
Lahiri A., Pochard P., Le Pottier L., Tobon G.J., Bendaoud B.,
Youinou P., Pers J.O.;
"The complexity of the BAFF TNF-family members: implications for
autoimmunity.";
J. Autoimmun. 39:189-198(2012).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Farrah T., Gross J., Piddington C., O'Hara P.;
"Homo sapiens homolog of tumor necrosis factor.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Dendritic cell;
Zhang W., Wan T., Yu Y., Cao X.;
"A novel dendritic cell-derived TNF-like molecule.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Gao H., He F., Li R.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135, AND VARIANT THR-105.
Kawasaki A., Tsuchiya N., Fukazawa T., Hashimoto H., Tokunaga K.;
"New polymorphisms of human BLyS gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[16]
FUNCTION.
PubMed=10973284; DOI=10.1038/79802;
Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M.,
McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M.,
Boyle W.J., Sarosi I., Hsu H., Senaldi G., Theill L.E.;
"APRIL and TALL-I and receptors BCMA and TACI: system for regulating
humoral immunity.";
Nat. Immunol. 1:252-256(2000).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 142-285.
PubMed=11853672; DOI=10.1016/S0092-8674(02)00631-1;
Liu Y., Xu L., Opalka N., Kappler J., Shu H.-B., Zhang G.;
"Crystal structure of sTALL-1 reveals a virus-like assembly of TNF
family ligands.";
Cell 108:383-394(2002).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 136-285.
PubMed=11827482; DOI=10.1006/jmbi.2001.5296;
Karpusas M., Cachero T.G., Qian F., Boriack-Sjodin A., Mullen C.,
Strauch K., Hsu Y.-M., Kalled S.L.;
"Crystal structure of extracellular human BAFF, a TNF family member
that stimulates B lymphocytes.";
J. Mol. Biol. 315:1145-1154(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-285.
PubMed=11862220; DOI=10.1038/nsb769;
Oren D.A., Li Y., Volovik Y., Morris T.S., Dharia C., Das K.,
Galperina O., Gentz R., Arnold E.;
"Structural basis of BLyS receptor recognition.";
Nat. Struct. Biol. 9:288-292(2002).
-!- FUNCTION: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA.
TNFSF13/APRIL binds to the same 2 receptors. Together, they form a
2 ligands -2 receptors pathway involved in the stimulation of
B- and T-cell function and the regulation of humoral immunity. A
third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the
survival of mature B-cells and the B-cell response.
{ECO:0000269|PubMed:10973284}.
-!- FUNCTION: Isoform 2 seems to inhibit isoform 1 secretion and
bioactivity. {ECO:0000250}.
-!- FUNCTION: Isoform 3: Acts as a transcription factor for its own
parent gene, in association with NF-kappa-B p50 subunit, at least
in autoimmune and proliferative B-cell diseases. The presence of
Delta4BAFF is essential for soluble BAFF release by IFNG/IFN-
gamma-stimulated monocytes and for B-cell survival. It can
directly or indirectly regulate the differential expression of a
large number of genes involved in the innate immune response and
the regulation of apoptosis. {ECO:0000269|PubMed:10973284}.
-!- SUBUNIT: Homotrimer. Isoform 2 heteromultimerizes with isoform 1,
probably limiting the amount of functional isoform 1 on the cell
surface. Isoform 3 is unlikely form trimers or bind to BAFF
receptors. {ECO:0000269|PubMed:12867412,
ECO:0000269|PubMed:22749832}.
-!- INTERACTION:
O14836:TNFRSF13B; NbExp=7; IntAct=EBI-519169, EBI-519160;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily
member 13b, soluble form: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y275-1; Sequence=Displayed;
Name=2; Synonyms=DeltaBAFF;
IsoId=Q9Y275-2; Sequence=VSP_041183;
Name=3; Synonyms=Delta4BAFF;
IsoId=Q9Y275-3; Sequence=VSP_047591, VSP_047592;
-!- TISSUE SPECIFICITY: Abundantly expressed in peripheral blood
Leukocytes and is specifically expressed in monocytes and
macrophages. Also found in the spleen, lymph node, bone marrow, T-
cells and dendritic cells. A lower expression seen in placenta,
heart, lung, fetal liver, thymus, and pancreas. Isoform 2 is
expressed in many myeloid cell lines.
{ECO:0000269|PubMed:12867412}.
-!- INDUCTION: Up-regulated by exposure to IFNG/IFN-gamma. Down-
regulated by phorbol myristate acetate/ionomycin treatment.
-!- PTM: The soluble form derives from the membrane form by
proteolytic processing.
-!- PTM: Isoform 2 is not efficiently shed from the membrane unlike
isoform 1. {ECO:0000250}.
-!- PTM: N-glycosylated.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue
77 of December 2006;
URL="https://web.expasy.org/spotlight/back_issues/077";
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EMBL; AF136293; AAD29421.1; -; mRNA.
EMBL; AF116456; AAD25356.1; -; mRNA.
EMBL; AF132600; AAD21092.1; -; mRNA.
EMBL; AY302751; AAP83164.1; -; mRNA.
EMBL; HM636064; ADK91575.1; -; mRNA.
EMBL; AF186114; AAF01432.1; -; mRNA.
EMBL; AF134715; AAF60219.1; -; mRNA.
EMBL; AY129225; AAN08421.1; -; mRNA.
EMBL; EF064706; ABK41889.1; -; Genomic_DNA.
EMBL; AY358881; AAQ89240.1; -; mRNA.
EMBL; CR541818; CAG46617.1; -; mRNA.
EMBL; AL157762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471085; EAX09099.1; -; Genomic_DNA.
EMBL; BC020674; AAH20674.1; -; mRNA.
EMBL; AB073225; BAB90856.1; -; Genomic_DNA.
CCDS; CCDS45067.1; -. [Q9Y275-2]
CCDS; CCDS9509.1; -. [Q9Y275-1]
RefSeq; NP_001139117.1; NM_001145645.2. [Q9Y275-2]
RefSeq; NP_006564.1; NM_006573.4. [Q9Y275-1]
UniGene; Hs.525157; -.
PDB; 1JH5; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=142-285.
PDB; 1KD7; X-ray; 2.80 A; A/B/C/K/L/M=133-285.
PDB; 1KXG; X-ray; 2.00 A; A/B/C/D/E/F=134-285.
PDB; 1OQD; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=142-285.
PDB; 1OQE; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=142-285.
PDB; 1OSG; X-ray; 3.00 A; A/B/C/D/E/F=82-285.
PDB; 3V56; X-ray; 3.00 A; A/B/C/D/E/F=82-285.
PDB; 4V46; X-ray; 3.30 A; A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/Aa/Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar/As/At/Au/Av/Aw/Ax=138-285.
PDB; 4ZCH; X-ray; 2.43 A; A/B=140-285.
PDBsum; 1JH5; -.
PDBsum; 1KD7; -.
PDBsum; 1KXG; -.
PDBsum; 1OQD; -.
PDBsum; 1OQE; -.
PDBsum; 1OSG; -.
PDBsum; 3V56; -.
PDBsum; 4V46; -.
PDBsum; 4ZCH; -.
ProteinModelPortal; Q9Y275; -.
SMR; Q9Y275; -.
BioGrid; 115915; 54.
CORUM; Q9Y275; -.
DIP; DIP-6225N; -.
IntAct; Q9Y275; 2.
STRING; 9606.ENSP00000365048; -.
ChEMBL; CHEMBL2364158; -.
DrugBank; DB08879; Belimumab.
DrugBank; DB04272; Citric Acid.
iPTMnet; Q9Y275; -.
PhosphoSitePlus; Q9Y275; -.
BioMuta; TNFSF13B; -.
DMDM; 13124573; -.
EPD; Q9Y275; -.
PaxDb; Q9Y275; -.
PeptideAtlas; Q9Y275; -.
PRIDE; Q9Y275; -.
DNASU; 10673; -.
Ensembl; ENST00000375887; ENSP00000365048; ENSG00000102524. [Q9Y275-1]
Ensembl; ENST00000430559; ENSP00000389540; ENSG00000102524. [Q9Y275-2]
Ensembl; ENST00000542136; ENSP00000445334; ENSG00000102524. [Q9Y275-3]
GeneID; 10673; -.
KEGG; hsa:10673; -.
UCSC; uc001vqr.4; human. [Q9Y275-1]
CTD; 10673; -.
DisGeNET; 10673; -.
EuPathDB; HostDB:ENSG00000102524.11; -.
GeneCards; TNFSF13B; -.
HGNC; HGNC:11929; TNFSF13B.
HPA; CAB009188; -.
MIM; 603969; gene.
neXtProt; NX_Q9Y275; -.
OpenTargets; ENSG00000102524; -.
PharmGKB; PA434; -.
eggNOG; ENOG410IHQ4; Eukaryota.
eggNOG; ENOG4111XFQ; LUCA.
GeneTree; ENSGT00530000063837; -.
HOGENOM; HOG000036810; -.
HOVERGEN; HBG061472; -.
InParanoid; Q9Y275; -.
KO; K05476; -.
OMA; MDDSTER; -.
OrthoDB; EOG091G0GBQ; -.
PhylomeDB; Q9Y275; -.
TreeFam; TF332331; -.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
SIGNOR; Q9Y275; -.
EvolutionaryTrace; Q9Y275; -.
GeneWiki; B-cell_activating_factor; -.
GenomeRNAi; 10673; -.
PRO; PR:Q9Y275; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102524; -.
CleanEx; HS_TNFSF13B; -.
ExpressionAtlas; Q9Y275; baseline and differential.
Genevisible; Q9Y275; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0031296; P:B cell costimulation; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0048305; P:immunoglobulin secretion; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:AgBase.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0002636; P:positive regulation of germinal center formation; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR006052; TNF_dom.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00229; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Membrane; Polymorphism; Reference proteome; Secreted; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 285 Tumor necrosis factor ligand superfamily
member 13b, membrane form.
/FTId=PRO_0000034528.
CHAIN 134 285 Tumor necrosis factor ligand superfamily
member 13b, soluble form.
/FTId=PRO_0000034529.
TOPO_DOM 1 46 Cytoplasmic. {ECO:0000255}.
TRANSMEM 47 67 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 68 285 Extracellular. {ECO:0000255}.
SITE 133 134 Cleavage.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
CARBOHYD 242 242 N-linked (GlcNAc...) (high mannose)
asparagine.
DISULFID 232 245
VAR_SEQ 142 160 Missing (in isoform 2).
{ECO:0000303|PubMed:12867412}.
/FTId=VSP_041183.
VAR_SEQ 162 164 SYT -> FIY (in isoform 3).
{ECO:0000303|PubMed:22749832}.
/FTId=VSP_047591.
VAR_SEQ 165 285 Missing (in isoform 3).
{ECO:0000303|PubMed:22749832}.
/FTId=VSP_047592.
VARIANT 105 105 A -> T (in dbSNP:rs201543678).
{ECO:0000269|Ref.15}.
/FTId=VAR_013483.
STRAND 146 151 {ECO:0000244|PDB:1KXG}.
STRAND 158 160 {ECO:0000244|PDB:1KXG}.
STRAND 163 165 {ECO:0000244|PDB:1KXG}.
STRAND 168 181 {ECO:0000244|PDB:1KXG}.
STRAND 184 187 {ECO:0000244|PDB:1KXG}.
STRAND 191 201 {ECO:0000244|PDB:1KXG}.
STRAND 205 215 {ECO:0000244|PDB:1KXG}.
TURN 219 222 {ECO:0000244|PDB:4ZCH}.
STRAND 225 235 {ECO:0000244|PDB:1KXG}.
STRAND 238 240 {ECO:0000244|PDB:1KXG}.
STRAND 243 253 {ECO:0000244|PDB:1KXG}.
STRAND 258 265 {ECO:0000244|PDB:1KXG}.
TURN 274 276 {ECO:0000244|PDB:1KXG}.
STRAND 277 283 {ECO:0000244|PDB:1KXG}.
SEQUENCE 285 AA; 31223 MW; 48ED0D7AB38C8867 CRC64;
MDDSTEREQS RLTSCLKKRE EMKLKECVSI LPRKESPSVR SSKDGKLLAA TLLLALLSCC
LTVVSFYQVA ALQGDLASLR AELQGHHAEK LPAGAGAPKA GLEEAPAVTA GLKIFEPPAP
GEGNSSQNSR NKRAVQGPEE TVTQDCLQLI ADSETPTIQK GSYTFVPWLL SFKRGSALEE
KENKILVKET GYFFIYGQVL YTDKTYAMGH LIQRKKVHVF GDELSLVTLF RCIQNMPETL
PNNSCYSAGI AKLEEGDELQ LAIPRENAQI SLDGDVTFFG ALKLL


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